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2ZNC

MURINE CARBONIC ANHYDRASE IV

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005791cellular_componentrough endoplasmic reticulum
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005886cellular_componentplasma membrane
A0006730biological_processone-carbon metabolic process
A0006885biological_processregulation of pH
A0008270molecular_functionzinc ion binding
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0015670biological_processcarbon dioxide transport
A0015701biological_processbicarbonate transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0016529cellular_componentsarcoplasmic reticulum
A0016829molecular_functionlyase activity
A0030658cellular_componenttransport vesicle membrane
A0030667cellular_componentsecretory granule membrane
A0031526cellular_componentbrush border membrane
A0042383cellular_componentsarcolemma
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0070062cellular_componentextracellular exosome
A0098552cellular_componentside of membrane
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AHIS94
AHIS96
AHIS119
AHOH264

site_idZN
Number of Residues3
DetailsZN BINDING SITE.
ChainResidue
AHIS94
AHIS96
AHIS119

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHsIdgrhFamEMHIV
ChainResidueDetails
ASER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS64

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9541386
ChainResidueDetails
AHIS94
AHIS96
AHIS119

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR199

site_idSWS_FT_FI4
Number of Residues1
DetailsLIPID: GPI-anchor amidated serine => ECO:0000250|UniProtKB:P22748
ChainResidueDetails
ASER259

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN103
AASN195

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR199
AHIS64

222926

PDB entries from 2024-07-24

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